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dc.contributor.authorReeks, Judith
dc.contributor.authorSokolowski, Richard D.
dc.contributor.authorGraham, Shirley
dc.contributor.authorLiu, Huanting
dc.contributor.authorNaismith, James H.
dc.contributor.authorWhite, Malcolm F.
dc.identifier.citationReeks , J , Sokolowski , R D , Graham , S , Liu , H , Naismith , J H & White , M F 2013 , ' Structure of a dimeric crenarchaeal Cas6 enzyme with an atypical active site for CRISPR RNA processing ' , Biochemical Journal , vol. 452 , no. 2 , pp. 223-230 .
dc.identifier.otherPURE: 58404836
dc.identifier.otherPURE UUID: 336c756b-4f1e-4338-82c6-416c02215416
dc.identifier.otherWOS: 000319635800005
dc.identifier.otherScopus: 84877757610
dc.identifier.otherORCID: /0000-0003-1543-9342/work/47136074
dc.descriptionThis work was funded by the Biotechnology and Biological Sciences Research Council [grant numbers BB/G011400/1 and BB/K000314/1 (to M.F.W. and J.H.N.)], a Biotechnology and Biological Sciences Research Council-funded studentship to J.R. and a Medical Research Council-funded studentship to R.D.S.en
dc.description.abstractThe competition between viruses and hosts is played out in all branches of life. Many prokaryotes have an adaptive immune system termed 'CRISPR' (clustered regularly interspaced short palindromic repeats) which is based on the capture of short pieces of viral DNA. The captured DNA is integrated into the genomic DNA of the organism flanked by direct repeats, transcribed and processed to generate crRNA (CRISPR RNA) that is loaded into a variety of effector complexes. These complexes carry out sequence-specific detection and destruction of invading mobile genetic elements. In the present paper, we report the structure and activity of a Cas6 (CRISPR-associated 6) enzyme (Sso1437) from Sulfolobus solfataricus responsible for the generation of unit-length crRNA species. The crystal structure reveals an unusual dimeric organization that is important for the enzyme's activity. In addition, the active site lacks the canonical catalytic histidine residue that has been viewed as an essential feature of the Cas6 family. Although several residues contribute towards catalysis, none is absolutely essential. Coupled with the very low catalytic rate constants of the Cas6 family and the plasticity of the active site, this suggests that the crRNA recognition and chaperone-like activities of the Cas6 family should be considered as equal to or even more important than their role as traditional enzymes.
dc.relation.ispartofBiochemical Journalen
dc.rights© 2013 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence ( which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.en
dc.subjectAntiviral defenceen
dc.subjectClustered regularly interspaced short palindromic repeats (CRISPR)en
dc.subjectDNA-binding proteinen
dc.subjectProcesses pre-CRRNAen
dc.subjectMacromolecular crystallographyen
dc.subjectQH426 Geneticsen
dc.titleStructure of a dimeric crenarchaeal Cas6 enzyme with an atypical active site for CRISPR RNA processingen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.description.statusPeer revieweden

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